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The protein encoded by RER1 is a multi-pass membrane protein that is localized to the golgi apparatus. Additionally we are shipping RER1 Antibodies (23) and many more products for this protein.
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Rer1p regulates the ER retention of immature or misfolded rhodopsin and modulates its intracellular trafficking through the early secretory pathway.
Charcot-Marie-Tooth disease-related PMP22 (show PMP22 Proteins) is trapped in the endoplasmic reticulum by calnexin (show CANX Proteins)-dependent retention and Rer1-mediated early Golgi retrieval systems and partly degraded by the Hrd1 (show SYVN1 Proteins)-mediated endoplasmic reticulum-associated degradation system.
Rer1p depletion reduced ciliary length and function by increasing gamma-secretase complex assembly and activity and, consequently, enhancing Notch (show NOTCH1 Proteins) signaling as well as reducing Foxj1a expression.
Synoviolin up-regulates amyloid beta production by targeting a negative regulator of gamma-secretase, Rer1, for degradation.
RER1 modulates amyloid-beta production by altering trafficking of gamma-secretase and amyloid precursor protein (show APP Proteins).
Downregulation of Rer1 leads to increased surface localization of Pen2 (show PSENEN Proteins), whereas overexpression of Rer1 stabilizes unassembled Pen2 (show PSENEN Proteins). Rer1 is the first identified interaction partner of mammalian transmembrane-based retention/retrieval signals.
Rer1 is a functionally important unique factor that controls surface expression of muscle acetylcholine receptors by localizing unassembled alpha-subunits to the early secretory pathway
The protein encoded by this gene is a multi-pass membrane protein that is localized to the golgi apparatus. It is involved in the retention of endoplasmic reticulum (ER) membrane proteins in the ER and retrieval of ER membrane proteins from the early Golgi compartment to facilitate gamma-secretase complex assembly.
RER1 retention in endoplasmic reticulum 1 homolog
, Protein RER1
, protein RER1
, RER1 protein